{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_17.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_15.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_08.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_13.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_19.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_16.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_18.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_05.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_14.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_20.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD062429/SgnC-1_09.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["timo.glatter@mpi-marburg.mpg.de"],"submitter":["Timo Glatter"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Myxococcus xanthus","Cell motolity","Mgla"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062429"],"tissue":["Permanent Cell Line Cell"],"sample_protocol":["To perform whole-cell proteomics experiments, a protocol based on (75) was used. Briefly, M. xanthus cells were grown on 1.5% agar plates supplemented with 1% CTT and appropriate antibiotics for 72hrs at 32°C. From these plates, 35 mg cells per replicate were washed with 500 μL 1x Pposphate-buffered saline (PBS) (137 mM NaCl, 2.7 mM KCl, 10 mM Na2HPO4, 1.8 mM KH2PO4, pH 7.5) supplemented with cOmplete EDTA-free Protease Inhibitor Cocktail Tablette (Roche) twice. Cells were lysed in 200 μL 2% (w/v) sodium lauroyl sarcosinate (SLS) with incubation at 95°C for 1h. After the cell debris was cleared, the supernatant was mixed with 1.2 mL freezer-cold acetone and incubated at -20°C overnight. Proteins were pelleted by centrifugation at 21000 x g for 15 min at 4°C. The protein pellets were washed with 750 μL freezer-cold methanol, dried, and the methanol completely removed. The precipitated protein pellet was solubilized using 200 μL 0.5% SLS and heat exposure. The protein amount was determined by bicinchoninic acid (BCA) assay (Thermo Fisher Scientific). Next, proteins were reduced using 5 mM Tris (2-carboxyethyl) phosphine (Thermo Fisher Scientific) at 90°C for 15 min and alkylated with 10 mM iodoacetamid (Sigma Aldrich) at 25°C for 30 min in the dark. 50 µg protein was digested using 1 µg trypsin (Serva) at 30°C overnight.  Following digestion, SLS was precipitated through acidification. Next, the peptides were desalted by using C18 solid phase extraction cartridges (Macherey-Nagel), which were prepared for loading the peptide sample by first adding acetonitrile (ACN), followed by 0.1% trifluoroacetic acid (TFA, Thermo Fisher Scientific). The cartridges were equilibrated, peptides were loaded, and washed with buffer containing 5% ACN/0.1percentage TFA. Peptides were eluted with 50% ACN and 0.1% TFA. Dried peptides were reconstituted in 0.1% TFA and then analyzed using liquid-chromatography-mass spectrometry (LC-MS) executed on an Ultimate 3000 RSLC nano connected to an Exploris 480 Mass Spectrometer (all Thermo Fisher Scientific) and a HPLC C18 column packed in-house (75 μm × 42 cm). Peptides were separated using the following gradient: 94% solvent A (0.15% formic acid) and 6% solvent B (99.85% acetonitrile, 0.15% formic acid) to 25% solvent B over 95 minutes at a flow rate of 300 nL min−1, followed by an additional increase of solvent B 35% over 25 min.  MS raw data was acquired in data-independent acquisition (DIA) mode. Briefly, the spray voltage was set to 2.3 kV, the funnel radio frequency level was set to 40, and the ion transfer capillary was heated to 275 °C. For DIA experiments, full MS resolutions were set to 120,000 at m/z 200 and full MS, with the AGC (automatic gain control) target set to 300 % and ion accumulation time (IT) of 50 ms. The AGC target value for fragment spectra was set to 3000%. 45 windows, each set to 14 Da plus 1 Da overlap, were used. The resolution was set to 15,000 with MS/MS IT to 22 ms. Stepped HCD high energy collision dissociation (HCD) collision energies of 25, 27.5, 30% were applied. MS1 data was acquired in profile mode, and MS2 DIA data in centroid mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["DIA data analysis was performed using the neural network (NN)-based DIA-NN suite version 1.8 (100) in combination with a M. xanthus protein database from UniProt. A dataset centric spectral library was generated for the DIA analysis. DIA-NN applied noise interference correction (mass correction, RT prediction and precursor/fragment co-elution correlation) and peptide precursor signal extraction from the raw DIA-NN data. The following settings were used for the analysis: Full tryptic digestion with two missed cleavage sites was allowed, with oxidized methionines and carbamidomethylated cysteines as modifications. “Match between runs” and “remove likely interferences” were enabled. The NN classifier was set to the single-pass mode, and protein inference was based on genes. Quantification was performed using the “any LC (high accuracy)” strategy, with cross-run normalization set to RT-dependent. Library generation was set to smart profiling. Outputs from DIA-NN were further evaluated using a SafeQuant (101, 102) script modified to process DIA-NN results."],"omics_type":["Proteomics"],"labhead":["Timo Glatter"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Max Planck Institute for Terrestrial Microbiology Karl-von-Frisch Str. 10  35043 Marburg Germany"],"species":["Myxococcus Xanthus Dk 1622"],"publication":["Not available"],"submitter_mail":["timo.glatter@mpi-marburg.mpg.de"],"submitter_affiliation":["Max Planck Institute for Terrestrial Microbiology\nMarburg"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"SgnC, a PATAN-domain response regulator, regulates Myxococcus xanthus motility","description":"Rod-shaped Myxococcus xanthus cells move across surfaces with defined front-rear polarity using type IVa pili (T4aP)-dependent motility and gliding. The M. xanthus genome encodes 15 PATAN domain proteins, including SgnC, SgmC, and PglH, which have been implicated in motility. Notably, six of these proteins contain a MshEN_N c-di-GMP binding motif as an α-clip insertion within the PATAN domain. Given the role of c-di-GMP in motility of M. xanthus, we characterized these proteins and found that MXAN3211, MXAN5196, and SgnC are important for both motility systems of M. xanthus, while MXAN4739 is specifically required for only T4aP-dependent motility. Next, we further investigated the molecular role of SgnC in motility of M. xanthus and found that SgnC inhibits cellular reversals in a Frz chemosensory system-dependent manner. This inhibition is independent of c-di-GMP binding of SgnC and not related to changes in the accumulation of motility-associated proteins. Surprisingly, SgnC was found to be close to the proteins that regulate T4aP formation, such as SgmX, FrzS, and SopA as revealed by our proximity labeling experiments. Consistently, our data support a direct interaction between SgnC and SgmX in vivo. Localization studies confirmed the previous findings regarding MglA, SgmX, and FrzS polar localization and demonstrated that SgnC affects the polar localization of SgmX directly, as well as MglA and PilB through its potential interaction with SgmX. In turn, proper SgmX localization is essential for SgnC polar localization.  Importantly, our data suggest that SgnC and SgmX reduce sensitivity to Frz chemosensory signaling by two distinct mechanisms. First, SgnC and SgmX stimulate MglA localization at the leading cell pole, which potentially shields MglA-GTP from the Frz signaling. Second, SgnC appears to inhibit the polar binding of the Frz effector FrzZ at the leading cell pole via an unknown mechanism. Together, our findings highlight SgnC as a novel regulator of M. xanthus motility, linking chemosensory signaling to T4aP 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